Summary for 3ZOI
| Entry DOI | 10.2210/pdb3zoi/pdb |
| Descriptor | ISOPENICILLIN N SYNTHASE, DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-O-METHYL-D-THREONINE, FE (III) ION, ... (6 entities in total) |
| Functional Keywords | oxidoreductase, b-lactam antibiotic, oxygenase, penicillin biosynthesis |
| Biological source | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Total number of polymer chains | 1 |
| Total formula weight | 38475.46 |
| Authors | Rutledge, P.J.,Clifton, I.J.,Ge, W. (deposition date: 2013-02-21, release date: 2013-06-26, Last modification date: 2024-05-08) |
| Primary citation | Clifton, I.J.,Ge, W.,Adlington, R.M.,Baldwin, J.E.,Rutledge, P.J. The Crystal Structure of an Isopenicillin N Synthase Complex with an Ethereal Substrate Analogue Reveals Water in the Oxygen Binding Site. FEBS Lett., 587:2705-, 2013 Cited by PubMed Abstract: Isopenicillin N synthase (IPNS) is a non-heme iron oxidase central to the biosynthesis of β-lactam antibiotics. IPNS converts the tripeptide δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (ACV) to isopenicillin N while reducing molecular oxygen to water. The substrate analogue δ-(L-α-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine (ACmT) is not turned over by IPNS. Epimeric δ-(L-α-aminoadipoyl)-L-cysteinyl-O-methyl-D-allo-threonine (ACmaT) is converted to a bioactive penam product. ACmT and ACmaT differ from each other only in the stereochemistry at the β-carbon atom of their third residue. These substrates both contain a methyl ether in place of the isopropyl group of ACV. We report an X-ray crystal structure for the anaerobic IPNS:Fe(II):ACmT complex. This structure reveals an additional water molecule bound to the active site metal, held by hydrogen-bonding to the ether oxygen atom of the substrate analogue. PubMed: 23860486DOI: 10.1016/J.FEBSLET.2013.07.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
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